Abstract
The gene products of the two major alleles of alcohol dehydrogenase (ADH-F and ADH-S) have been subjected to kinetic and biochemical analyses over a range of temperatures. Although temperature was found to have a significant effect on both kinetic and biochemical properties ofDrosophila ADH, no significant differential effect was observed between the major ADH allozymes. The results are discussed within the context of the selective maintenance ofAdh polymorphism in natural populations.
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Alahiotis, S. N. (1982). Adaptation ofDrosophila enzymes to temperature. IV. Natural selection at the alcohol-dehydrogenase locus.Genetica 5981.
Anderson, S. M., and McDonald, J. F. (1981a). A method for determining thein vivo stability ofDrosophila alcohol dehydrogenase (EC 1.1.1.1).Biochem. Genet. 19411.
Anderson, S. M., and McDonald, J. F. (1981b). Effect of environmental alcohol onin vivo properties ofDrosophila alcohol dehydrogenase.Biochem. Genet. 19421.
Anderson, S. M., and McDonald, J. F. (1981c). Changes in levels of alcohol dehydrogenase during the development ofDrosophila melanogaster.Can. J. Genet. Cytol. 23305.
Anderson, S. M., and McDonald, J. F. (1983). Biochemical and molecular analysis of naturally occurring Adh variants inDrosophila melanogaster.Proc. Natl. Acad. Sci. USA 804798.
Anderson, S. M., Santos, M., and McDonald, J. F. (1980). Comparative study of the thermostability of crude and purified preparations of alcohol dehydrogenase (EC 1.1.1.1) fromD. melanogaster.Dros. Info. Serv. 5513.
Anderson, S. M., McDonald, J. F., and Santos, M. (1981). Selection at the Adh locus inDrosophila melanogaster: Adult survivorship-mortality in response to ethanol.Experientia 37463.
Benyajati, C., Place, A. R., Powers, D. A., and Sofer, W. (1981). Alcohol dehydrogenase gene ofDrosophila melanogaster: Relationship of intervening sequences to functional domains in the protein.Proc. Natl. Acad. Sci. USA 782717.
Cavener, D. R., and Clegg, M. T. (1981). Multigenic response to ethanol inDrosophila melanogaster.Evolution 351.
Cleland, W. W. (1979). Statistical analysis of enzyme kinetic data.Meth. Enzymol. 63A103.
Cornish-Bowden, A. (1979).Fundamentals of Enzyme Kinetics Butterworths, Boston, Chap. 10.
Cornish-Bowden, A., and Endrenyi, L. (1981). Fitting of enzyme kinetic data without prior knowledge of weights.Biochem. J. 1931005.
David, J. L., Bocquet, C., Arens, M., and Fouillett, P. (1976). Biological role of alcohol dehydrogenase in the tolerance ofDrosophila melanogaster to aliphatic alcohols: Utilization of an ADH-null mutant.Biochem. Genet. 14989.
Davis, B. J. (1964). Disc electrophoresis. II. Method and application to human serum proteins.Ann. N.Y. Acad. Sci. 121404.
Day, T. H., and Needham, L. (1974). Properties of alcohol dehydrogenase isozymes in a strain ofDrosophila melanogaster homozygous for the ADH-slow allele.Biochem. Genet. 11:167.
Day, T. H., Hillier, P. C., and Clarke, B. (1974). Properties of genetically polymorphic isozymes of alcohol dehydrogenase inDrosophila melanogaster.Biochem. Genet. 11141.
Everse, J., Zoll, L., Kahan, L., and Kaplan, N. (1971). Addition products of diphosphopyridine nucleotides with substrates of pyridine nucleotide linked dehydrogenases.Bioorgan. Chem. 1207.
Grell, E. H., Jacobson, K. B., and Murphy, J. (1965). Alcohol dehydrogenase inDrosophila melanogaster: Isozymes and genetic variants.Science 14980.
Fersht, A. R. (1977).Enzyme Structure and Mechanism W. H. Freeman, San Francisco.
Fromm, H. J. (1975).Initial Rate Kinetics Springer-Verlag, Berlin.
Hochachka, P. W., and Somero, G. N. (1973).Strategies of Biochemical Adaptation W. B. Saunders, Philadelphia, Chap. 7.
Jacobson, K. B. (1968). Alcohol dehydrogenase ofDrosophila: Interconversion of isozymes.Science 159324.
King, J. J., and McDonald, J. F. (1983). Genetic localization and biochemical characterization of a trans-acting regulatory effect inDrosophila.Genetics 10555.
Laemmli, U. K. (1970). Cleavage of structural proteins during the assembly of the head of bacteria phage T4.Nature 227685.
McDonald, J. F. (1983). The molecular basis of adaptation: A critical review of relevant ideas and observations.Annu. Rev. Ecol. System. 1477.
McDonald, J. F., and Avise, J. C. (1976). Evidence for the adaptive significance of enzyme activity levels. Interspecific variation in α-glycerol phosphate dehydrogenase and alcohol dehydrogenase inDrosophila.Biochem. Genet. 14347.
McDonald, J. F., and Ayala, F. J. (1978). Genetic and biochemical basis of enzyme variation in natural populations I. Alcohol dehydrogenase inD. melanogaster.Genetics 89371.
McDonald, J. F., Chambers, G., David, J., and Ayala, F. J. (1977). Adaptive response due to changes in gene regulation: A study withDrosophila.Proc. Natl. Acad. Sci. USA 744562.
McDonald, J. F., Anderson, S. M., and Santos, M. (1980). Biochemical differences between products of the ADH locus inDrosophila.Genetics 951013.
McElfresh, K. C., and McDonald, J. F. (1983). The effect of alcohol stress on micotinamide adenine dinucleotide (NAD+) levels inDrosophila.Biochem. Genet. 21365.
Mosteller, F., and Tukey, J. W. (1977).Data Analysis and Regression Addison-Wesley, Reading, Mass., p. 333.
Oakeshott, J., Gibson, J., Anderson, P., Knibb, W., Anderson, D., and Chambers, G. (1982). Alcohol dehydrogenase and glycerol-3-phosphate dehydrogenase clines inD. melanogaster on different continents.Evolution 3686.
Ornstein, L. (1964). Disc electrophoresis. I. Background and theory.Ann. N.Y. Acad. Sci. 121321.
Sampsell, B. (1977). Isolation and genetic characterization of alcohol dehydrogenase thermostability variants occurring in natural populations ofDrosophila melanogaster.Biochem. Genet. 15971.
Sampsell, B., and Sims, S. (1982). Effect ofadh genotype and heat stress on alcohol tolerance inDrosophila melanogaster.Nature 296853.
Schwartz, M., and Sofer, W. (1976). Diet-induced alterations in distributions of multiple forms of alcohol dehydrogenase inDrosophila.Nature 263129.
Schwartz, M., O'Donnell, J., and Sofer, W. (1979). Origin of the multiple forms of alcohol dehydrogenase fromDrosophila melanogaster.Arch. Biochem. Biophys. 194365.
Smith, I. (1968). Acrylamide gel electrophoresis. In Smith, E. (ed.),Chromatographic and Electrophoretic Techniques Interscience, New York, p. 365.
Shadravan, F., and McDonald, J. (1986). The secondary product threshold model andAdh polymorphism inDrosophila (submitted for publication).
Thatcher, D. R., and Shiekh, R. (1981). The relative conformational stability of the alcohol dehydrogenase allenzymes of the fruitflyDrosophila melanogaster.Biochem. J. 197111.
Ursprung, H., and Leone, J. (1965). Alcohol dehydrogenase: A polymorphism inDrosophila melanogaster.J. Exp. Zool. 160147.
van Delden, W. A. (1982). The alcohol dehydrogenase polymorphism inDrosophila melanogaster. Selection at an enzyme locus. In Hecht, M., Wallace, B., and Prance, G. T. (eds.),Selection at an Enzyme Locus, Evolutionary Biology Vol. 15, p. 187.
van Delden, W. A., and Kamping, A. (1980). The alcohol dehydrogenase polymorphism ofD. melanogaster. IV. Survival at high temperature.Genetica 51179.
van Delden, W. A., Boerema, A. C., and Kamping, A. (1978). The alcohol dehydrogenase polymorphism in populations ofDrosophila melanogaster. I. Selection in different environments.Genetics 90164.
Vigue, C. L., and Johnson, F. M. (1973). Isozyme variability of the genusDrosophila. VI. Frequency-property-environment relationships of allelic alcohol dehydrogenases inD. melanogaster.Biochem. Genet. 9213.
Wilkinson, G. N. (1961). Statistical estimations in enzyme kinetics.Biochem. J. 80324.
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A significant portion of the calculations was made possible by a grant from DECOR (1982) which provided a PDP-11/34 minicomputer to the Department of Genetics, University of Georgia. This work was supported by NSF Grant DEB-82-00965 to J.M.
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McElfresh, K.C., McDonald, J.F. The effect of temperature on biochemical and molecular properties ofDrosophila alcohol dehydrogenase. Biochem Genet 24, 873–889 (1986). https://doi.org/10.1007/BF00554526
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DOI: https://doi.org/10.1007/BF00554526